메뉴 건너뛰기




Volumn 18, Issue 3, 2010, Pages 132-139

Functional diversity of ankyrin repeats in microbial proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; BACTERIAL PROTEIN; PROTEIN ANKA; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 77649148783     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2009.11.004     Document Type: Review
Times cited : (172)

References (92)
  • 1
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?
    • Bork P. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?. Proteins 17 (1993) 363-364
    • (1993) Proteins , vol.17 , pp. 363-364
    • Bork, P.1
  • 2
    • 18744380008 scopus 로고    scopus 로고
    • Consensus-derived structural determinants of the ankyrin repeat motif
    • Mosavi L.K., Minor Jr. D.L., and Peng Z.Y. Consensus-derived structural determinants of the ankyrin repeat motif. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16029-16034
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16029-16034
    • Mosavi, L.K.1    Minor Jr., D.L.2    Peng, Z.Y.3
  • 3
    • 20244372135 scopus 로고    scopus 로고
    • Intracellular cAMP controls a physical association of V-1 with CapZ in cultured mammalian endocrine cells
    • Kitazawa M., et al. Intracellular cAMP controls a physical association of V-1 with CapZ in cultured mammalian endocrine cells. Biochem. Biophys. Res. Commun. 331 (2005) 181-186
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 181-186
    • Kitazawa, M.1
  • 4
    • 0032905860 scopus 로고    scopus 로고
    • X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals variations of the ankyrin fold and has implications for Swi6 function
    • Foord R., et al. X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals variations of the ankyrin fold and has implications for Swi6 function. Nat. Struct. Biol. 6 (1999) 157-165
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 157-165
    • Foord, R.1
  • 5
    • 17744366374 scopus 로고    scopus 로고
    • The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold
    • Lubman O.Y., et al. The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold. Protein Sci. 14 (2005) 1274-1281
    • (2005) Protein Sci. , vol.14 , pp. 1274-1281
    • Lubman, O.Y.1
  • 6
    • 0023280623 scopus 로고
    • Similarity between cell-cycle genes of budding yeast and fission yeast and the Notch gene of Drosophila
    • Breeden L., and Nasmyth K. Similarity between cell-cycle genes of budding yeast and fission yeast and the Notch gene of Drosophila. Nature 329 (1987) 651-654
    • (1987) Nature , vol.329 , pp. 651-654
    • Breeden, L.1    Nasmyth, K.2
  • 7
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi L.K., et al. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 13 (2004) 1435-1448
    • (2004) Protein Sci. , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1
  • 8
    • 40249108385 scopus 로고    scopus 로고
    • [Functional role of proteins containing ankyrin repeats]
    • Voronin D.A., and Kiseleva E.V. [Functional role of proteins containing ankyrin repeats]. Tsitologiia 49 (2007) 989-999
    • (2007) Tsitologiia , vol.49 , pp. 989-999
    • Voronin, D.A.1    Kiseleva, E.V.2
  • 9
    • 38549146894 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Finn R.D., et al. The Pfam protein families database. Nucleic Acids Res. 36 Suppl_1 (2008) D281-288
    • (2008) Nucleic Acids Res. , vol.36 , Issue.SUPPL. 1
    • Finn, R.D.1
  • 10
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: recent updates and new developments
    • Letunic I., et al. SMART 6: recent updates and new developments. Nucleic Acids Res. 37 Suppl 1 (2009) D229-232
    • (2009) Nucleic Acids Res. , vol.37 , Issue.SUPPL. 1
    • Letunic, I.1
  • 11
    • 58149203231 scopus 로고    scopus 로고
    • InterPro: the integrative protein signature database
    • Hunter S., et al. InterPro: the integrative protein signature database. Nucleic Acids Res. 37 Suppl 1 (2009) D211-215
    • (2009) Nucleic Acids Res. , vol.37 , Issue.SUPPL. 1
    • Hunter, S.1
  • 12
    • 35648945780 scopus 로고    scopus 로고
    • Ankyrin repeat domain-encoding genes in the wPip strain of Wolbachia from the Culex pipiens group
    • Walker T., et al. Ankyrin repeat domain-encoding genes in the wPip strain of Wolbachia from the Culex pipiens group. BMC Biol. 5 (2007) 39
    • (2007) BMC Biol. , vol.5 , pp. 39
    • Walker, T.1
  • 13
    • 46249111623 scopus 로고    scopus 로고
    • Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors
    • Pan X., et al. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science 320 (2008) 1651-1654
    • (2008) Science , vol.320 , pp. 1651-1654
    • Pan, X.1
  • 14
    • 0037452697 scopus 로고    scopus 로고
    • Designed to be stable: crystal structure of a consensus ankyrin repeat protein
    • Kohl A., et al. Designed to be stable: crystal structure of a consensus ankyrin repeat protein. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1700-1705
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1700-1705
    • Kohl, A.1
  • 15
    • 0035890072 scopus 로고    scopus 로고
    • Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family
    • Michel F., et al. Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family. Embo J. 20 (2001) 6180-6190
    • (2001) Embo J. , vol.20 , pp. 6180-6190
    • Michel, F.1
  • 16
    • 5444222526 scopus 로고    scopus 로고
    • Ankyrin repeat-containing proteins in Arabidopsis: characterization of a novel and abundant group of genes coding ankyrin-transmembrane proteins
    • Becerra C., et al. Ankyrin repeat-containing proteins in Arabidopsis: characterization of a novel and abundant group of genes coding ankyrin-transmembrane proteins. Gene 340 (2004) 111-121
    • (2004) Gene , vol.340 , pp. 111-121
    • Becerra, C.1
  • 17
    • 27644527039 scopus 로고    scopus 로고
    • Sequence variation in ligand binding sites in proteins
    • Magliery T.J., and Regan L. Sequence variation in ligand binding sites in proteins. BMC Bioinformatics 6 (2005) 240
    • (2005) BMC Bioinformatics , vol.6 , pp. 240
    • Magliery, T.J.1    Regan, L.2
  • 18
    • 33845934490 scopus 로고    scopus 로고
    • ankyrin repeat: a unique motif mediating protein-protein interactions
    • Li J., et al. ankyrin repeat: a unique motif mediating protein-protein interactions. Biochemistry 45 (2006) 15168-15178
    • (2006) Biochemistry , vol.45 , pp. 15168-15178
    • Li, J.1
  • 19
    • 33644849450 scopus 로고    scopus 로고
    • Nanospring behaviour of ankyrin repeats
    • Lee G., et al. Nanospring behaviour of ankyrin repeats. Nature 440 (2006) 246-249
    • (2006) Nature , vol.440 , pp. 246-249
    • Lee, G.1
  • 20
    • 43749107950 scopus 로고    scopus 로고
    • Mechanical biochemistry of proteins one molecule at a time
    • Oberhauser A.F., and Carrion-Vazquez M. Mechanical biochemistry of proteins one molecule at a time. J. Biol. Chem 283 (2008) 6617-6621
    • (2008) J. Biol. Chem , vol.283 , pp. 6617-6621
    • Oberhauser, A.F.1    Carrion-Vazquez, M.2
  • 21
    • 33746690468 scopus 로고    scopus 로고
    • The F-box protein family
    • REVIEWS3002
    • Kipreos E.T., and Pagano M. The F-box protein family. Genome Biol. 1 (2000) REVIEWS3002
    • (2000) Genome Biol. , vol.1
    • Kipreos, E.T.1    Pagano, M.2
  • 22
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B., and Kajava A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11 (2001) 725-732
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 23
    • 40449095056 scopus 로고    scopus 로고
    • Evolution of protein domain promiscuity in eukaryotes
    • Basu M.K., et al. Evolution of protein domain promiscuity in eukaryotes. Genome Res. 18 (2008) 449-461
    • (2008) Genome Res. , vol.18 , pp. 449-461
    • Basu, M.K.1
  • 24
    • 0026806912 scopus 로고
    • Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm
    • Bennett V. Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem 267 (1992) 8703-8706
    • (1992) J. Biol. Chem , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 25
    • 0242291971 scopus 로고    scopus 로고
    • Genomic analysis of secretion systems
    • Pallen M.J., et al. Genomic analysis of secretion systems. Curr. Opin. Microbiol 6 (2003) 519-527
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 519-527
    • Pallen, M.J.1
  • 26
    • 60049091769 scopus 로고    scopus 로고
    • ESX/type VII secretion systems and their role in host-pathogen interaction
    • Simeone R., et al. ESX/type VII secretion systems and their role in host-pathogen interaction. Curr. Opin. Microbiol. 12 (2009) 4-10
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 4-10
    • Simeone, R.1
  • 27
    • 70349277187 scopus 로고    scopus 로고
    • The structural biology of type IV secretion systems
    • Fronzes R., et al. The structural biology of type IV secretion systems. Nat. Rev. Microbiol. 7 (2009) 703-714
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 703-714
    • Fronzes, R.1
  • 28
    • 70350734524 scopus 로고    scopus 로고
    • Imaging the assembly, structure and activity of type III secretion systems
    • Enninga J., and Rosenshine I. Imaging the assembly, structure and activity of type III secretion systems. Cell Microbiol. 11 (2009) 1462-1470
    • (2009) Cell Microbiol. , vol.11 , pp. 1462-1470
    • Enninga, J.1    Rosenshine, I.2
  • 29
    • 67649400561 scopus 로고    scopus 로고
    • Common themes in the design and function of bacterial effectors
    • Galan J.E. Common themes in the design and function of bacterial effectors. Cell Host Microbe 5 (2009) 571-579
    • (2009) Cell Host Microbe , vol.5 , pp. 571-579
    • Galan, J.E.1
  • 30
    • 60849116153 scopus 로고    scopus 로고
    • Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology
    • Tseng T.T., et al. Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology. BMC Microbiol. 9 Suppl 1 (2009) S2
    • (2009) BMC Microbiol. , vol.9 , Issue.SUPPL. 1
    • Tseng, T.T.1
  • 31
    • 54249166663 scopus 로고    scopus 로고
    • A Dot/Icm-translocated ankyrin protein of Legionella pneumophila is required for intracellular proliferation within human macrophages and protozoa
    • Al-Khodor S., et al. A Dot/Icm-translocated ankyrin protein of Legionella pneumophila is required for intracellular proliferation within human macrophages and protozoa. Mol. Microbiol. 70 (2008) 908-923
    • (2008) Mol. Microbiol. , vol.70 , pp. 908-923
    • Al-Khodor, S.1
  • 32
    • 34848862803 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection
    • Lin M., et al. Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection. Cell Microbiol. 9 (2007) 2644-2657
    • (2007) Cell Microbiol. , vol.9 , pp. 2644-2657
    • Lin, M.1
  • 33
    • 34147154867 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection
    • IJdo J., et al. Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection. Cell Microbiol. 9 (2007) 1284-1296
    • (2007) Cell Microbiol. , vol.9 , pp. 1284-1296
    • IJdo, J.1
  • 34
    • 0036112267 scopus 로고    scopus 로고
    • Type IVB secretion by intracellular pathogens
    • Sexton J.A., and Vogel J. Type IVB secretion by intracellular pathogens. Traffic 3 (2002) 178-185
    • (2002) Traffic , vol.3 , pp. 178-185
    • Sexton, J.A.1    Vogel, J.2
  • 35
    • 18344402639 scopus 로고    scopus 로고
    • AnkB, a periplasmic ankyrin-like protein in Pseudomonas aeruginosa, is required for optimal catalase B (KatB) activity and resistance to hydrogen peroxide
    • Howell M.L., et al. AnkB, a periplasmic ankyrin-like protein in Pseudomonas aeruginosa, is required for optimal catalase B (KatB) activity and resistance to hydrogen peroxide. J. Bacteriol. 182 (2000) 4545-4556
    • (2000) J. Bacteriol. , vol.182 , pp. 4545-4556
    • Howell, M.L.1
  • 36
    • 33745727547 scopus 로고    scopus 로고
    • Anaplasma and Ehrlichia infection
    • Dumler J.S. Anaplasma and Ehrlichia infection. Ann. N. Y. Acad. Sci. 1063 (2005) 361-373
    • (2005) Ann. N. Y. Acad. Sci. , vol.1063 , pp. 361-373
    • Dumler, J.S.1
  • 37
    • 0033850294 scopus 로고    scopus 로고
    • ankA: an Ehrlichia phagocytophila group gene encoding a cytoplasmic protein antigen with ankyrin repeats
    • Caturegli P., et al. ankA: an Ehrlichia phagocytophila group gene encoding a cytoplasmic protein antigen with ankyrin repeats. Infect. Immun. 68 (2000) 5277-5283
    • (2000) Infect. Immun. , vol.68 , pp. 5277-5283
    • Caturegli, P.1
  • 38
    • 4143085008 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins
    • Park J., et al. Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins. Cell Microbiol. 6 (2004) 743-751
    • (2004) Cell Microbiol. , vol.6 , pp. 743-751
    • Park, J.1
  • 39
    • 66549089938 scopus 로고    scopus 로고
    • Silencing of host cell CYBB gene expression by the nuclear effector AnkA of the intracellular pathogen Anaplasma phagocytophilum
    • Garcia-Garcia J.C., et al. Silencing of host cell CYBB gene expression by the nuclear effector AnkA of the intracellular pathogen Anaplasma phagocytophilum. Infect. Immun. 77 (2009) 2385-2391
    • (2009) Infect. Immun. , vol.77 , pp. 2385-2391
    • Garcia-Garcia, J.C.1
  • 40
    • 48849086594 scopus 로고    scopus 로고
    • Proteomic analysis of and immune responses to Ehrlichia chaffeensis lipoproteins
    • Huang H., et al. Proteomic analysis of and immune responses to Ehrlichia chaffeensis lipoproteins. Infect. Immun. 76 (2008) 3405-3414
    • (2008) Infect. Immun. , vol.76 , pp. 3405-3414
    • Huang, H.1
  • 41
    • 0026598520 scopus 로고
    • The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding
    • Hatada E.N., et al. The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 2489-2493
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 2489-2493
    • Hatada, E.N.1
  • 42
    • 0027472317 scopus 로고
    • The NF-kappa B precursor p105 and the proto-oncogene product Bcl-3 are I kappa B molecules and control nuclear translocation of NF-kappa B
    • Naumann M., et al. The NF-kappa B precursor p105 and the proto-oncogene product Bcl-3 are I kappa B molecules and control nuclear translocation of NF-kappa B. Embo J. 12 (1993) 213-222
    • (1993) Embo J. , vol.12 , pp. 213-222
    • Naumann, M.1
  • 43
    • 0038051506 scopus 로고    scopus 로고
    • Novel Immunoreactive glycoprotein orthologs of Ehrlichia spp
    • McBride J.W., et al. Novel Immunoreactive glycoprotein orthologs of Ehrlichia spp. Ann. N. Y. Acad. Sci. 990 (2003) 678-684
    • (2003) Ann. N. Y. Acad. Sci. , vol.990 , pp. 678-684
    • McBride, J.W.1
  • 44
    • 70349417835 scopus 로고    scopus 로고
    • Nuclear translocated Ehrlichia chaffeensis ankyrin protein interacts with a specific adenine-rich motif of host promoter and intronic Alu elements
    • Zhu B., et al. Nuclear translocated Ehrlichia chaffeensis ankyrin protein interacts with a specific adenine-rich motif of host promoter and intronic Alu elements. Infect. Immun. 77 (2009) 4243-4255
    • (2009) Infect. Immun. , vol.77 , pp. 4243-4255
    • Zhu, B.1
  • 45
    • 33746377600 scopus 로고    scopus 로고
    • Alu elements contain many binding sites for transcription factors and may play a role in regulation of developmental processes
    • Polak P., and Domany E. Alu elements contain many binding sites for transcription factors and may play a role in regulation of developmental processes. BMC Genomics. 7 (2006) 133
    • (2006) BMC Genomics. , vol.7 , pp. 133
    • Polak, P.1    Domany, E.2
  • 46
    • 12244295183 scopus 로고    scopus 로고
    • Amoebae as training grounds for intracellular bacterial pathogens
    • Molmeret M., et al. Amoebae as training grounds for intracellular bacterial pathogens. Appl. Environ. Microbiol. 71 (2005) 20-28
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 20-28
    • Molmeret, M.1
  • 47
    • 0030833998 scopus 로고    scopus 로고
    • Utilization of similar mechanisms by Legionella pneumophila to parasitize two evolutionarily distant hosts, mammalian and protozoan cells
    • Gao L.-Y., et al. Utilization of similar mechanisms by Legionella pneumophila to parasitize two evolutionarily distant hosts, mammalian and protozoan cells. Infect. Immun. 65 (1997) 4738-4746
    • (1997) Infect. Immun. , vol.65 , pp. 4738-4746
    • Gao, L.-Y.1
  • 48
    • 0035691622 scopus 로고    scopus 로고
    • How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane
    • Tilney L.G., et al. How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane. J. Cell Sci. 114 Pt 24 (2001) 4637-4650
    • (2001) J. Cell Sci. , vol.114 , Issue.PART 24 , pp. 4637-4650
    • Tilney, L.G.1
  • 49
    • 0036327647 scopus 로고    scopus 로고
    • The road less traveled: transport of Legionella to the endoplasmic reticulum
    • Roy C.R., and Tilney L.G. The road less traveled: transport of Legionella to the endoplasmic reticulum. J. Cell Biol. 158 (2002) 415-419
    • (2002) J. Cell Biol. , vol.158 , pp. 415-419
    • Roy, C.R.1    Tilney, L.G.2
  • 50
    • 18844421402 scopus 로고    scopus 로고
    • [What do we learn from the genome of Legionella pneumophila?]
    • Cazalet C., and Buchrieser C. [What do we learn from the genome of Legionella pneumophila?]. Med. Sci. (Paris) 21 (2005) 455-457
    • (2005) Med. Sci. (Paris) , vol.21 , pp. 455-457
    • Cazalet, C.1    Buchrieser, C.2
  • 51
    • 44349121198 scopus 로고    scopus 로고
    • Identification and characterization of a new conjugation/type IVA secretion system (trb/tra) of Legionella pneumophila Corby localized on two mobile genomic islands
    • Glockner G., et al. Identification and characterization of a new conjugation/type IVA secretion system (trb/tra) of Legionella pneumophila Corby localized on two mobile genomic islands. Int J. Med. Microbiol. 298 (2008) 411-428
    • (2008) Int J. Med. Microbiol. , vol.298 , pp. 411-428
    • Glockner, G.1
  • 52
    • 43449096622 scopus 로고    scopus 로고
    • Role for the ankyrin eukaryotic-like genes of Legionella pneumophila in parasitism of protozoan hosts and human macrophages
    • Habyarimana F., et al. Role for the ankyrin eukaryotic-like genes of Legionella pneumophila in parasitism of protozoan hosts and human macrophages. Environ Microbiol. 10 (2008) 1460-1474
    • (2008) Environ Microbiol. , vol.10 , pp. 1460-1474
    • Habyarimana, F.1
  • 53
    • 27744546297 scopus 로고    scopus 로고
    • Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer
    • De Felipe K.S., et al. Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer. J. Bacteriol. 187 (2005) 7716-7726
    • (2005) J. Bacteriol. , vol.187 , pp. 7716-7726
    • De Felipe, K.S.1
  • 54
    • 27144522274 scopus 로고    scopus 로고
    • Convergent evolution as a mechanism for pathogenic adaptation
    • Sikora S., et al. Convergent evolution as a mechanism for pathogenic adaptation. Trends Microbiol. 13 (2005) 522-527
    • (2005) Trends Microbiol. , vol.13 , pp. 522-527
    • Sikora, S.1
  • 55
    • 50849115482 scopus 로고    scopus 로고
    • Legionella eukaryotic-like type IV substrates interfere with organelle trafficking
    • de Felipe K.S., et al. Legionella eukaryotic-like type IV substrates interfere with organelle trafficking. PLoS Pathog 4 (2008) e1000117
    • (2008) PLoS Pathog , vol.4
    • de Felipe, K.S.1
  • 56
    • 77349095439 scopus 로고    scopus 로고
    • Habyarimana, F. et al. (2010) Molecular characterization of the Dot/Icm-translocated AnkH and AnkJ eukaryotic-like effectors of Legionella pneumophila. Infect. Immun., in press
    • Habyarimana, F. et al. (2010) Molecular characterization of the Dot/Icm-translocated AnkH and AnkJ eukaryotic-like effectors of Legionella pneumophila. Infect. Immun., in press
  • 57
    • 0030918480 scopus 로고    scopus 로고
    • Golgi membrane skeleton: identification, localization and oligomerization of a 195 kDa ankyrin isoform associated with the Golgi complex
    • Beck K.A., et al. Golgi membrane skeleton: identification, localization and oligomerization of a 195 kDa ankyrin isoform associated with the Golgi complex. J. Cell Sci. 110 Pt 10 (1997) 1239-1249
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 10 , pp. 1239-1249
    • Beck, K.A.1
  • 58
    • 74549200971 scopus 로고    scopus 로고
    • Price, C.T. et al. (2009) Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa. PLoS Pathog. 5, e1000704
    • Price, C.T. et al. (2009) Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa. PLoS Pathog. 5, e1000704
  • 59
    • 0036784707 scopus 로고    scopus 로고
    • Coxiella burnetii localizes in a Rab7-labeled compartment with autophagic characteristics
    • Beron W., et al. Coxiella burnetii localizes in a Rab7-labeled compartment with autophagic characteristics. Infect. Immun. 70 (2002) 5816-5821
    • (2002) Infect. Immun. , vol.70 , pp. 5816-5821
    • Beron, W.1
  • 60
    • 11844273940 scopus 로고    scopus 로고
    • The Icm/Dot type-IV secretion systems of Legionella pneumophila and Coxiella burnetii
    • Segal G., et al. The Icm/Dot type-IV secretion systems of Legionella pneumophila and Coxiella burnetii. FEMS Microbiol. Rev. 29 (2005) 65-81
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 65-81
    • Segal, G.1
  • 61
    • 0038649869 scopus 로고    scopus 로고
    • Functional similarities between the icm/dot pathogenesis systems of Coxiella burnetii and Legionella pneumophila
    • Zusman T., et al. Functional similarities between the icm/dot pathogenesis systems of Coxiella burnetii and Legionella pneumophila. Infect. Immun. 71 (2003) 3714-3723
    • (2003) Infect. Immun. , vol.71 , pp. 3714-3723
    • Zusman, T.1
  • 62
    • 67649397592 scopus 로고    scopus 로고
    • The Coxiella burnetii ankyrin repeat domain-containing protein family is heterogeneous, with C-terminal truncations that influence Dot/Icm-mediated secretion
    • Voth D.E., et al. The Coxiella burnetii ankyrin repeat domain-containing protein family is heterogeneous, with C-terminal truncations that influence Dot/Icm-mediated secretion. J. Bacteriol. 191 (2009) 4232-4422
    • (2009) J. Bacteriol. , vol.191 , pp. 4232-4422
    • Voth, D.E.1
  • 63
    • 60549105201 scopus 로고    scopus 로고
    • Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella
    • Beare P.A., et al. Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella. Infect. Immun. 77 (2009) 642-656
    • (2009) Infect. Immun. , vol.77 , pp. 642-656
    • Beare, P.A.1
  • 64
    • 0033818145 scopus 로고    scopus 로고
    • Long PCR improves Wolbachia DNA amplification: wsp sequences found in 76% of sixty-three arthropod species
    • Jeyaprakash A., and Hoy M.A. Long PCR improves Wolbachia DNA amplification: wsp sequences found in 76% of sixty-three arthropod species. Insect MolBiol. 9 (2000) 393-405
    • (2000) Insect MolBiol. , vol.9 , pp. 393-405
    • Jeyaprakash, A.1    Hoy, M.A.2
  • 65
    • 0029660819 scopus 로고    scopus 로고
    • Wolbachia: intracellular manipulators of mite reproduction
    • Breeuwer J.A., and Jacobs G. Wolbachia: intracellular manipulators of mite reproduction. ExpApplAcarol. 20 (1996) 421-434
    • (1996) ExpApplAcarol. , vol.20 , pp. 421-434
    • Breeuwer, J.A.1    Jacobs, G.2
  • 66
    • 0032557941 scopus 로고    scopus 로고
    • Evidence for widespread Wolbachia infection in isopod crustaceans: molecular identification and host feminization
    • Bouchon D., et al. Evidence for widespread Wolbachia infection in isopod crustaceans: molecular identification and host feminization. Proc. Biol. Sci. 265 (1998) 1081-1090
    • (1998) Proc. Biol. Sci. , vol.265 , pp. 1081-1090
    • Bouchon, D.1
  • 67
    • 0032722408 scopus 로고    scopus 로고
    • Wolbachia pipientis: microbial manipulator of arthropod reproduction
    • Stouthamer R., et al. Wolbachia pipientis: microbial manipulator of arthropod reproduction. Annu. Rev. Microbiol. 53 (1999) 71-102
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 71-102
    • Stouthamer, R.1
  • 68
    • 19344378727 scopus 로고    scopus 로고
    • Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements
    • Wu M., et al. Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements. PLoS Biol. 2 (2004) E69
    • (2004) PLoS Biol. , vol.2
    • Wu, M.1
  • 69
    • 49749134637 scopus 로고    scopus 로고
    • Genome evolution of Wolbachia strain wPip from the Culex pipiens group
    • Klasson L., et al. Genome evolution of Wolbachia strain wPip from the Culex pipiens group. Mol. Biol. Evol. 25 (2008) 1877-1887
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1877-1887
    • Klasson, L.1
  • 70
    • 39049085373 scopus 로고    scopus 로고
    • Wolbachia genome integrated in an insect chromosome: evolution and fate of laterally transferred endosymbiont genes
    • Nikoh N., et al. Wolbachia genome integrated in an insect chromosome: evolution and fate of laterally transferred endosymbiont genes. Genome Res. 18 (2008) 272-280
    • (2008) Genome Res. , vol.18 , pp. 272-280
    • Nikoh, N.1
  • 71
    • 0033604517 scopus 로고    scopus 로고
    • The complete DNA sequence of myxoma virus
    • Cameron C., et al. The complete DNA sequence of myxoma virus. Virology 264 (1999) 298-318
    • (1999) Virology , vol.264 , pp. 298-318
    • Cameron, C.1
  • 72
    • 38149111916 scopus 로고    scopus 로고
    • The role of cell signaling in poxvirus tropism: the case of the M-T5 host range protein of myxoma virus
    • Werden S.J., and McFadden G. The role of cell signaling in poxvirus tropism: the case of the M-T5 host range protein of myxoma virus. Biochim. Biophys. Acta. 1784 (2008) 228-237
    • (2008) Biochim. Biophys. Acta. , vol.1784 , pp. 228-237
    • Werden, S.J.1    McFadden, G.2
  • 73
    • 49449090299 scopus 로고    scopus 로고
    • Poxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexes
    • Sonnberg S., et al. Poxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexes. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 10955-10960
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10955-10960
    • Sonnberg, S.1
  • 74
    • 33846176872 scopus 로고    scopus 로고
    • Characterization of the IkappaB-like gene family in polydnaviruses associated with wasps belonging to different Braconid subfamilies
    • Falabella P., et al. Characterization of the IkappaB-like gene family in polydnaviruses associated with wasps belonging to different Braconid subfamilies. J. Gen. Virol. 88 Pt 1 (2007) 92-104
    • (2007) J. Gen. Virol. , vol.88 , Issue.PART 1 , pp. 92-104
    • Falabella, P.1
  • 75
    • 33847209578 scopus 로고    scopus 로고
    • M-T5, the ankyrin repeat, host range protein of myxoma virus, activates Akt and can be functionally replaced by cellular PIKE-A
    • Werden S.J., et al. M-T5, the ankyrin repeat, host range protein of myxoma virus, activates Akt and can be functionally replaced by cellular PIKE-A. J. Virol. 81 (2007) 2340-2348
    • (2007) J. Virol. , vol.81 , pp. 2340-2348
    • Werden, S.J.1
  • 76
    • 23244452458 scopus 로고    scopus 로고
    • Myxoma virus M-T5 protects infected cells from the stress of cell cycle arrest through its interaction with host cell cullin-1
    • Johnston J.B., et al. Myxoma virus M-T5 protects infected cells from the stress of cell cycle arrest through its interaction with host cell cullin-1. J. Virol. 79 (2005) 10750-10763
    • (2005) J. Virol. , vol.79 , pp. 10750-10763
    • Johnston, J.B.1
  • 77
    • 33645240416 scopus 로고    scopus 로고
    • Infection of human cancer cells with myxoma virus requires Akt activation via interaction with a viral ankyrin-repeat host range factor
    • Wang G., et al. Infection of human cancer cells with myxoma virus requires Akt activation via interaction with a viral ankyrin-repeat host range factor. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 4640-4645
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4640-4645
    • Wang, G.1
  • 78
    • 42649139905 scopus 로고    scopus 로고
    • The highly conserved orthopoxvirus 68k ankyrin-like protein is part of a cellular SCF ubiquitin ligase complex
    • Sperling K.M., et al. The highly conserved orthopoxvirus 68k ankyrin-like protein is part of a cellular SCF ubiquitin ligase complex. Virology 374 (2008) 234-239
    • (2008) Virology , vol.374 , pp. 234-239
    • Sperling, K.M.1
  • 79
    • 53749106941 scopus 로고    scopus 로고
    • Ectromelia virus encodes a novel family of F-box proteins that interact with the SCF complex
    • van Buuren N., et al. Ectromelia virus encodes a novel family of F-box proteins that interact with the SCF complex. J. Virol. 82 (2008) 9917-9927
    • (2008) J. Virol. , vol.82 , pp. 9917-9927
    • van Buuren, N.1
  • 80
    • 0036546501 scopus 로고    scopus 로고
    • NF-kappaB in cancer: from innocent bystander to major culprit
    • Karin M., et al. NF-kappaB in cancer: from innocent bystander to major culprit. Nat. Rev. Cancer. 2 (2002) 301-310
    • (2002) Nat. Rev. Cancer. , vol.2 , pp. 301-310
    • Karin, M.1
  • 81
    • 1242296946 scopus 로고    scopus 로고
    • A virulence factor of myxoma virus colocalizes with NF-kappaB in the nucleus and interferes with inflammation
    • Camus-Bouclainville C., et al. A virulence factor of myxoma virus colocalizes with NF-kappaB in the nucleus and interferes with inflammation. J. Virol. 78 (2004) 2510-2516
    • (2004) J. Virol. , vol.78 , pp. 2510-2516
    • Camus-Bouclainville, C.1
  • 82
    • 0036050851 scopus 로고    scopus 로고
    • Perspectives on polydnavirus origins and evolution
    • Turnbull M., and Webb B. Perspectives on polydnavirus origins and evolution. Adv. Virus Res. 58 (2002) 203-254
    • (2002) Adv. Virus Res. , vol.58 , pp. 203-254
    • Turnbull, M.1    Webb, B.2
  • 83
    • 34447521655 scopus 로고    scopus 로고
    • Cloning and characterization of two Campoletis chlorideae ichnovirus vankyrin genes expressed in parasitized host Helicoverpa armigera
    • Tian S.P., et al. Cloning and characterization of two Campoletis chlorideae ichnovirus vankyrin genes expressed in parasitized host Helicoverpa armigera. J. Insect Physiol. 53 (2007) 699-707
    • (2007) J. Insect Physiol. , vol.53 , pp. 699-707
    • Tian, S.P.1
  • 84
    • 3943069115 scopus 로고    scopus 로고
    • Mechanical processes in biochemistry
    • Bustamante C., et al. Mechanical processes in biochemistry. Annu. Rev. Biochem. 73 (2004) 248-705
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 248-705
    • Bustamante, C.1
  • 85
    • 37349036497 scopus 로고    scopus 로고
    • Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments
    • Interlandi G., et al. Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments. J. Mol. Biol. 375 (2008) 837-854
    • (2008) J. Mol. Biol. , vol.375 , pp. 837-854
    • Interlandi, G.1
  • 86
    • 67651094146 scopus 로고    scopus 로고
    • Selection and characterization of DARPins specific for the neurotensin receptor 1
    • Milovnik P., et al. Selection and characterization of DARPins specific for the neurotensin receptor 1. Protein Eng. Des. Sel. 22 (2009) 357-366
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 357-366
    • Milovnik, P.1
  • 87
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution - a structural perspective
    • Orengo C.A., and Thornton J.M. Protein families and their evolution - a structural perspective. Annu Rev. Biochem. 74 (2005) 867-900
    • (2005) Annu Rev. Biochem. , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 88
    • 0037079014 scopus 로고    scopus 로고
    • The structure of the protein universe and genome evolution
    • Koonin E.V., et al. The structure of the protein universe and genome evolution. Nature 420 (2002) 218-223
    • (2002) Nature , vol.420 , pp. 218-223
    • Koonin, E.V.1
  • 89
    • 26244442102 scopus 로고    scopus 로고
    • Modules, multidomain proteins and organismic complexity
    • Tordai H., et al. Modules, multidomain proteins and organismic complexity. FEBS J. 272 (2005) 5064-5078
    • (2005) FEBS J. , vol.272 , pp. 5064-5078
    • Tordai, H.1
  • 90
    • 0034625235 scopus 로고    scopus 로고
    • The impact of comparative genomics on our understanding of evolution
    • Koonin E.V., et al. The impact of comparative genomics on our understanding of evolution. Cell 101 (2000) 573-576
    • (2000) Cell , vol.101 , pp. 573-576
    • Koonin, E.V.1
  • 91
    • 0034634395 scopus 로고    scopus 로고
    • The evolutionary fate and consequences of duplicate genes
    • Lynch M., and Conery J.S. The evolutionary fate and consequences of duplicate genes. Science. 290 (2000) 1151-1155
    • (2000) Science. , vol.290 , pp. 1151-1155
    • Lynch, M.1    Conery, J.S.2
  • 92
    • 0029567019 scopus 로고
    • Mechanism for binding site diversity on ankyrin. Comparison of binding sites on ankyrin for neurofascin and the Cl-/HCO3- anion exchanger
    • Michaely P., and Bennett V. Mechanism for binding site diversity on ankyrin. Comparison of binding sites on ankyrin for neurofascin and the Cl-/HCO3- anion exchanger. J. Biol. Chem. 270 (1995) 31298-31302
    • (1995) J. Biol. Chem. , vol.270 , pp. 31298-31302
    • Michaely, P.1    Bennett, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.